ID A0A2K5Y5M7_MANLE Unreviewed; 1229 AA.
AC A0A2K5Y5M7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=DHX38 {ECO:0000313|Ensembl:ENSMLEP00000010863.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000010863.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000010863.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC PRP16 sub-subfamily. {ECO:0000256|ARBA:ARBA00038040}.
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DR AlphaFoldDB; A0A2K5Y5M7; -.
DR Ensembl; ENSMLET00000034282.1; ENSMLEP00000010863.1; ENSMLEG00000029417.1.
DR GeneTree; ENSGT00940000156898; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17983; DEXHc_DHX38; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140}.
FT DOMAIN 537..700
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 722..904
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1229 AA; 140432 MW; 32CB2360C3A35E00 CRC64;
MGDTSEDASI HRLEGTDLDS QVGGLICKTK SAASEQHVFK APAPRPSLLG LDLLASLKRR
EREEKDDGED KKKSKISSYK DWEEGKDDQK DAEEEGGDQA GRNIRKDRHY RSARVETPSH
PGGVSEEFWE RSRQRERERR EHGVYASSKE EKDWKKEKSM GCMFLNDRDR SRHSSRSERD
GGSERSSRRN EPESPRHRPK DAATPSRSTW EEEDSGYGSS RRSQWESPSP TPSYRDSERS
HRLSTRDRDR SVRGKYSDDT PLPTPSYKYN EWADDRRHLG STPRLSRGRG RREEGEEGIS
FDTEEERQQW EDDQRQADRD WYMMDEGYDE FHNPLAYSSE DYVRRREQHL HKQKQKRISA
QRRQINEDNE RWETNRMLTS GVVHRLEVDE DFEEDNAAKV HLMVHNLVPP FLDGRIVFTK
QPEPVIPVKD ATSDLAIIAR KGSQTVRKHR EQKERKKAQH KHWELAGTKL GDIMGVKKEE
EPDKAVTEDG KVDYRTEQKF ADHMKKKSEA SSEFAKKKSI LEQRQYLPIF AVQQELLTII
RDNSIVIVVG ETGSGKTTQL TQYLHEDGYT DYGMIGCTQP RRVAAMSVAK RVSEEMGGNL
GEEVGYAIRF EDCTSENTLI KYMTDGILLR ESLREADLDH YSAIIMDEAH ERSLNTDVLF
GLLREVVARR SDLKLIVTSA TMDAEKFAAF FGNVPIFHIP GRTFPVDILF SKTPQEDYVE
AAVKQSLQVH LSGAPGDILI FMPGQEDIEV TSDQIVEHLE ELENAPALAV LPIYSQLPSD
LQAKIFQKVL SCLEGLIFPS LYCIVATNIA ETSLTVDGIM FVIDSGYCKL KVFNPRIGMD
ALQIYPISQA NANQRSGRAG RTGPGQCFRL YTQSAYKNEL LTTTVPEIQR TNLANVVLLL
KSLGVQDLLQ FHFMDPPPED NMLNSMYQLW ILGALDNTGG LTSTGRLMVE FPLDPALSKM
LIVSCDMGCS SEILLIVSML SVPAIFYRPK GREEESDQIR EKFAVPESDH LTYLNVYLQW
KNNNYSTIWC NDHFIHAKAM RKVREVRAQL KDIMVQQRMS LASCGTDWDI VRKCICAAYF
HQAAKLKGIG EYVNIRTGMP CHLHPTSSLF GMGYTPDYIV YHELVMTTKE YMQCVTAVDG
EWLAELGPMF YSVKQAGKSR QENRRRAKEE ASAMEEEMAL AEEQLRARRQ EQEKRSPLGS
VRSTKIYTPG RKEQGEPMTP RRTPARFGL
//
